Sensitivity-Enhanced Multidimensional Solid-State NMR Spectroscopy by Optimal-Control-Based Transverse Mixing Sequences

0561460 - ÚOCHB 2023 RIV US eng J - Článek v odborném periodiku
Blahut, Jan - Brandl, M. J. - Pradhan, T. - Reif, B. - Tošner, Z.
Sensitivity-Enhanced Multidimensional Solid-State NMR Spectroscopy by Optimal-Control-Based Transverse Mixing Sequences.
Journal of the American Chemical Society. Roč. 144, č. 38 (2022), s. 17336-17340. ISSN 0002-7863. E-ISSN 1520-5126
Výzkumná infrastruktura: e-INFRA CZ - 90140; CIISB II - 90127
Institucionální podpora: RVO:61388963
Klíčová slova: distance measurements * proteins * improvement
Obor OECD: Atomic, molecular and chemical physics (physics of atoms and molecules including collision, interaction with radiation, magnetic resonances, Mössbauer effect)
Impakt faktor: 15, rok: 2022
Způsob publikování: Omezený přístup
https://doi.org/10.1021/jacs.2c06568

Recently, proton-detected magic-angle spinning (MAS) solid-state nuclear magnetic resonance (NMR) spectroscopy has become an attractive tool to study the structure and dynamics of insoluble proteins at atomic resolution. The sensitivity of the employed multidimensional experiments can be systematically improved when both transversal components of the magnetization are transferred simultaneously after an evolution period. The method of preservation of equivalent pathways has been explored in solution-state NMR, however, it does not find widespread application due to relaxation issues connected with increased molecular size. We present here for the first time heteronuclear transverse mixing sequences for correlation experiments at moderate and fast MAS frequencies. Optimal control allows to boost the signal-to-noise ratio (SNR) beyond the expected factor of root 2 for each indirect dimension. In addition to the carbon-detected sensitivity-enhanced 2D NCA experiment, we present a novel proton-detected, doubly sensitivity-enhanced 3D hCANH pulse sequence for which we observe a 3-fold improvement in SNR compared to the conventional experimental implementation. The sensitivity gain turned out to be essential to unambiguously characterize a minor fibril polymorph of a human lambda-III immunoglobulin light chain protein that escaped detection so far.
Trvalý link: https://hdl.handle.net/11104/0334075